This is the structure of proteins that is the 3d structure due to noncovalent interactions between amino acid R groups (subunit interactions)

Tertiary structure

What are the interactions between R chains that can cause tertiary structure to form?

All proteins have a primary structure, and most have a secondary structure. Larger proteins can have a tertiary and quarternary structure. Of these proteins, there are two main broad categories:

Globular and Fibrous

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This category of proteins is somewhat water soluble, has many fxns: enzymes, hormones, membrane pumps/channels/receptors, inter and intracellular storage and transport, osmotic regulation, immune response, etc

Globular Proteins

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This category of proteins is not water soluble, made from long polymers, maintain + add strength to cellular and matrix structure

Fibrous proteins

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_____ proteins are mostly comprised of secondary structure

_____ proteins are mostly comprised of tertiary structure

Fibrous

Globular

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DNA is a polymer of ______

nucleotides

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What are the parts of a nucleotide?

Nitrogen base, five carbon sugar deoxyribose, and a phosphate group

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What are the purines?

What are the pyrimidines?

Adenine, guanine = purines

cytosine, thymine = pyrdimidines

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Which nitrogen base pair has 3 H-bonds?

Which has two?

C-G

A-T

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What is the name for a nucleic acid structure which is only comprised of a sugar and nitrogen base?

nucleoside

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DNA is comprised of two ANTIPARALLEL/PARALLEL strands of a double helix

Antiparallel

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RNA is a polymer of nucleotides that contain ___, not ____

What nitrogen base is replaced by uracil in RNA?

ribose, not deoxyribose

Thymine (pairs with adenine)

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Is RNA usually single or double stranded

RNA is usually single stranded

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What are the 4 principles of cell doctrine/theory?

1. All living organisms are composed of one or more cells. 2. The cell is the basic unit of structure, function, andorganization in all organisms.3. All cells come from preexisting, living cells. 4. Cells carry hereditary information

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This theory proposes that self-replicating ribonucleic acid (RNA) molecules were precursors to current life (based ondeoxyribonucleic acid (DNA), RNA and proteins).

RNA world hypothesis

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RNA STORES GENETIC INFORMATION like DNA and CATALYZES CHEMICAL REACTIONS like an ENZYME protein, so it may have played a major step in the evolution of cellular life.

RNA is unstable STABLE/UNSTABLE compared to DNA, so more likely toparticipate in chemical rxns (due to its extra hydroxyl group).

RNA world hypothesis

RNA is unstable compared to DNA, due to its hydroxyl group, so it is more likely to participate in chemical reactions

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What is the central dogma of genetics?

iological information cannot be transferred back from protein to either protein or nucleic acid;

DNA ->RNA -> proteins

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Which type of microscopy is basic, the phase contrast doesn't kill or stain tissue?

Light microscopy

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This type of microscopy is high magnification and resolution but kills tissue (scanning and magnification)

Electron Microscopes

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This type of microscopy is used to observe chromosomes during mitosis

Fluorescence microscopy

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Centrifugation spins and separates liquified cell homogenates into layers based upon

Which layer is the most dense?

What's next?

What's next?

Density

Nuclei Layer

Mitochondria

Ribosomes

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How do catalysts accelerate the rate of a rxn?

They lower the activation energy

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Metabolism =

catabolism + anabolism + energy transfer

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Concentration of ___ and _____ determines which way a rxn will go

Reactants and products

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When the rate of forward and reverse rxns is the same, there is 0 net production, and the reaction is in

Equilibrium

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Enzymes are ___ proteins that act as catalysts

They are specific for what?

Do enzymes change after a reaction?

Do they only catalyze reactions in the forward direction?

Where do substrates bind enzymes? What occurs?

Globular

Substrate

No.

No, both forward and reverse

The substrates binds at the active site. Induced fit occurs.

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Cofactors are nonprotein molecules that assist enzymes usually by donating or accepting some component of arxn like....

These are organic cofactors that usually donate or accept electrons

electrons

Coenzymes

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Are vitamins coenzymes or metallic ions?

Inorganic cofactors are usually _____

If metal ions bind covalently, it becomes a

Coenzymes

metal ions

Prosthetic group

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This is a common source of activation energy

How is new ATP formed (what reaction)?

ATP

Phosphorylation

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ATP is formed from _______ + phosphate using energy from an energy rich molecule like _____

ADP

Glucose

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Is ATP potential energy?

No, but it contains potential energy

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These are enzymes that have both an active site for substrate binding and an allosteric site for the binding of an allosteric effector (activator or inhibitor)

Allosteric Enzymes

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This is a substance that mimics the substrate and thereby inhibits the enzyme by binding the active site.

It's effects can be overcome by

Competitive Inhibitor

Increased substrate concentration

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What changes with competitive enzymes?

Kmax is increased, Vmax is unaffected

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This is a substance that inhibits enzyme binding by binding elsewhere than the active site of an enzyme, the substrate can still bind.

Noncompetitive Inhibition

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What changes in noncompetitive inhibition?

Km is unchanged, Vmax decreases

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This is the property of enzymes where the enzyme becomes more receptive to additional substrate molecules after one substrate molecule attaches to an active site

What class of structures is this usually seen in?

What was the example in class?

Cooperativity

Quaternary - enzymes with multiple subunits that each have an active site